LEU11_ARATH
ID LEU11_ARATH Reviewed; 631 AA.
AC Q9LPR4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 2.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=2-isopropylmalate synthase 1, chloroplastic;
DE EC=2.3.3.13 {ECO:0000269|PubMed:17189332};
DE AltName: Full=Methylthioalkylmalate synthase-like 4;
DE Flags: Precursor;
GN Name=IPMS1; Synonyms=MAML-4; OrderedLocusNames=At1g18500;
GN ORFNames=F15H18.3;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP FUNCTION.
RX PubMed=15155874; DOI=10.1104/pp.104.039347;
RA Field B., Cardon G., Traka M., Botterman J., Vancanneyt G., Mithen R.;
RT "Glucosinolate and amino acid biosynthesis in Arabidopsis.";
RL Plant Physiol. 135:828-839(2004).
RN [4]
RP FUNCTION, SUBUNIT, ACTIVITY REGULATION, CATALYTIC ACTIVITY, COFACTOR,
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=17189332; DOI=10.1104/pp.106.085555;
RA de Kraker J.-W., Luck K., Textor S., Tokuhisa J.G., Gershenzon J.;
RT "Two Arabidopsis genes (IPMS1 and IPMS2) encode isopropylmalate synthase,
RT the branchpoint step in the biosynthesis of leucine.";
RL Plant Physiol. 143:970-986(2007).
RN [5]
RP NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=17369439; DOI=10.1104/pp.106.091579;
RA Textor S., de Kraker J.-W., Hause B., Gershenzon J., Tokuhisa J.G.;
RT "MAM3 catalyzes the formation of all aliphatic glucosinolate chain lengths
RT in Arabidopsis.";
RL Plant Physiol. 144:60-71(2007).
CC -!- FUNCTION: Catalyzes the condensation of the acetyl group of acetyl-CoA
CC with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-
CC hydroxy-4-methylpentanoate (2-isopropylmalate). Involved in Leu
CC biosynthesis, but do not participate in the chain elongation of
CC glucosinolates. {ECO:0000269|PubMed:15155874,
CC ECO:0000269|PubMed:17189332}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-
CC isopropylmalate + CoA + H(+); Xref=Rhea:RHEA:21524, ChEBI:CHEBI:1178,
CC ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.13;
CC Evidence={ECO:0000269|PubMed:17189332};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17189332};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC -!- ACTIVITY REGULATION: Feedback inhibition by Leu.
CC {ECO:0000269|PubMed:17189332}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=304 uM for 3-methyl-2-oxobutanoate {ECO:0000269|PubMed:17189332};
CC KM=45 uM for acetyl-CoA {ECO:0000269|PubMed:17189332};
CC Vmax=2300 umol/min/g enzyme with 3-methyl-2-oxobutanoate as substrate
CC {ECO:0000269|PubMed:17189332};
CC Vmax=2100 umol/min/g enzyme with acetyl-CoA as substrate
CC {ECO:0000269|PubMed:17189332};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:17189332};
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 1/4. {ECO:0000305|PubMed:17189332}.
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:17189332}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers and
CC siliques. {ECO:0000269|PubMed:17189332}.
CC -!- DEVELOPMENTAL STAGE: Induced in seeds during silique ripening.
CC {ECO:0000269|PubMed:17189332}.
CC -!- DISRUPTION PHENOTYPE: Plants show an increased Val content but no
CC changes in Leu content. {ECO:0000269|PubMed:17189332}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. LeuA type 1 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF26002.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC013354; AAF26002.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29723.1; -; Genomic_DNA.
DR RefSeq; NP_173285.2; NM_101708.3.
DR AlphaFoldDB; Q9LPR4; -.
DR SMR; Q9LPR4; -.
DR BioGRID; 23670; 7.
DR STRING; 3702.AT1G18500.1; -.
DR iPTMnet; Q9LPR4; -.
DR PaxDb; Q9LPR4; -.
DR PRIDE; Q9LPR4; -.
DR ProteomicsDB; 250739; -.
DR EnsemblPlants; AT1G18500.1; AT1G18500.1; AT1G18500.
DR GeneID; 838431; -.
DR Gramene; AT1G18500.1; AT1G18500.1; AT1G18500.
DR KEGG; ath:AT1G18500; -.
DR Araport; AT1G18500; -.
DR TAIR; locus:2014179; AT1G18500.
DR eggNOG; KOG2367; Eukaryota.
DR HOGENOM; CLU_022158_0_1_1; -.
DR InParanoid; Q9LPR4; -.
DR OMA; NTMRMLV; -.
DR OrthoDB; 928619at2759; -.
DR PhylomeDB; Q9LPR4; -.
DR BRENDA; 2.3.3.13; 399.
DR UniPathway; UPA00048; UER00070.
DR PRO; PR:Q9LPR4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LPR4; baseline and differential.
DR Genevisible; Q9LPR4; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IDA:TAIR.
DR GO; GO:0009098; P:leucine biosynthetic process; IDA:TAIR.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.30.160.270; -; 1.
DR HAMAP; MF_01025; LeuA_type1; 1.
DR InterPro; IPR013709; 2-isopropylmalate_synth_dimer.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR InterPro; IPR005671; LeuA_bact_synth.
DR InterPro; IPR000891; PYR_CT.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF08502; LeuA_dimer; 1.
DR SMART; SM00917; LeuA_dimer; 1.
DR SUPFAM; SSF110921; SSF110921; 1.
DR TIGRFAMs; TIGR00973; leuA_bact; 1.
DR PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Chloroplast; Leucine biosynthesis; Plastid; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..57
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 58..631
FT /note="2-isopropylmalate synthase 1, chloroplastic"
FT /id="PRO_0000315839"
FT DOMAIN 89..362
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT REGION 59..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 631 AA; 68676 MW; 8213076F7E16B2A8 CRC64;
MASSLLRNPN LYSSTTITTT SFLPTFSSKP TPISSSFRFQ PSHHRSISLR SQTLRLSCSI
SDPSPLPPHT PRRPRPEYIP NRISDPNYVR VFDTTLRDGE QSPGATLTSK EKLDIARQLA
KLGVDIIEAG FPAASKDDFE AVKTIAETVG NTVDENGYVP VICGLSRCNK KDIERAWDAV
KYAKRPRIHT FIATSDIHLE YKLKKTKAEV IEIARSMVRF ARSLGCEDVE FSPEDAGRSE
REYLYEILGE VIKAGATTLN IPDTVGITLP SEFGQLITDL KANTPGIENV VISTHCQNDL
GLSTANTLSG AHAGARQMEV TINGIGERAG NASLEEVVMA IKCRGDHVLG GLFTGIDTRH
IVMTSKMVEE YTGMQTQPHK AIVGANAFAH ESGIHQDGML KHKGTYEIIC PEEIGLERSN
DAGIVLGKLS GRHALKDRLT ELGYQLDDEQ LSTIFWRFKT VAEQKKRVTD ADIIALVSDE
VFQPEAVWKL LDIQITCGTL GLSTATVKLA DADGKEHVAC SIGTGPVDSA YKAVDLIVKE
PATLLEYSMN AVTEGIDAIA TTRVLIRGSN KYSSTNAITG EEVQRTFSGT GAGMDIVVSS
VKAYVGALNK MMDFKENSAT KIPSQKNRVA A
